CJC-1295 No DAC & Ipamorelin

CJC-1295 No DAC & Ipamorelin

CJC-1295 No DAC & Ipamorelin is a combination research preparation that pairs the 30–amino acid growth hormone–releasing hormone analog CJC-1295 (No DAC) with the selective growth hormone secretagogue Ipamorelin. The two peptides act through complementary receptor systems on pituitary somatotrophs—CJC-1295 (No DAC) via GHRH receptors and Ipamorelin via ghrelin (GHS-R1a) receptors—to support coordinated, pulsatile growth hormone (GH) release and subsequent insulin-like growth factor 1 (IGF-1) production.

Because the CJC-1295 component is in its non–DAC-conjugated form, this combination retains a shorter biological half-life and promotes discrete, physiologic GH pulses rather than sustained hormone elevation. This makes CJC-1295 No DAC & Ipamorelin suitable for experimental use in models of GH/IGF-1 axis regulation, pulsatile endocrine signaling, anabolic metabolism, and tissue regeneration under conditions that approximate natural GH secretory patterns.

CJC-1295 No DAC & Ipamorelin Overview

In this dual-peptide system, CJC-1295 (No DAC) is a synthetic analog derived from the native GHRH(1–29) fragment, incorporating four targeted amino acid substitutions at positions 2, 8, 15, and 27 to enhance structural stability and resistance to enzymatic degradation while preserving physiologic receptor affinity. Ipamorelin, a highly selective growth hormone secretagogue, activates ghrelin receptors to further enhance GH release when used in conjunction with GHRH analogs.

The absence of a Drug Affinity Complex (DAC) linkage on CJC-1295 shortens its plasma half-life and favors transient, pulsatile GH secretion. When combined with Ipamorelin’s GHS-mediated stimulation, CJC-1295 No DAC & Ipamorelin provides a flexible experimental framework for investigating synergistic GH-axis modulation, metabolism, tissue repair, and body-composition changes in controlled preclinical studies designed to mimic physiologic GH oscillations.

CJC-1295 (No DAC) Research

Growth Hormone Stimulation and Mechanism of Action

CJC-1295 (No DAC) is a synthetic analog of growth hormone–releasing hormone (GHRH 1-29) engineered to preserve potent receptor activity while exhibiting improved resistance to enzymatic degradation. Through four targeted amino acid substitutions, the peptide maintains high receptor affinity for GHRH receptors expressed on pituitary somatotrophs, thereby stimulating the pulsatile secretion of growth hormone (GH).

Unlike sustained agonists or DAC-conjugated derivatives that extend GH elevation over prolonged periods, the No DAC variant produces discrete, physiologically relevant GH pulses. This pattern aligns closely with natural endocrine rhythms, avoiding the receptor desensitization and negative feedback that can accompany continuous GH stimulation. Preclinical findings have demonstrated a clear dose-dependent increase in GH and subsequent IGF-1 release, providing a controlled framework for investigating anabolic and metabolic regulation.

Metabolic and Body Composition Research

Experimental studies involving CJC-1295 (No DAC) have shown notable increases in serum GH and IGF-1 concentrations, which are central mediators of lipid metabolism, lean tissue growth, and nutrient partitioning. These effects contribute to research exploring reductions in adiposity, improvements in nitrogen retention, and maintenance of lean body mass.

Combination studies using CJC-1295 (No DAC) with growth hormone secretagogues (GHS) such as Ipamorelin or GHRP-6 demonstrate synergistic potentiation of GH pulse amplitude and frequency. This synergy allows researchers to model physiological and pharmacological mechanisms governing energy expenditure, glucose utilization, mitochondrial activity, and cellular repair. Such dual-peptide protocols are frequently utilized in studies of metabolic efficiency, muscle recovery, and age-related sarcopenia models.

Neurological and Regenerative Research Applications

The GH/IGF-1 signaling axis extends beyond somatic growth, influencing neurogenesis, synaptic plasticity, and neural repair. Laboratory models employing CJC-1295 (No DAC) have been used to study neuronal proliferation, glial modulation, and vascular remodeling, processes critical to cognitive function and neural tissue recovery following injury.

Furthermore, GH and IGF-1 pathways are implicated in connective-tissue remodeling, collagen synthesis, and angiogenesis—making this peptide valuable in regenerative-medicine frameworks investigating wound healing, musculoskeletal regeneration, and post-injury recovery. By preserving a physiologic pattern of GH stimulation, CJC-1295 (No DAC) provides a controlled environment to evaluate these tissue-repair processes without the confounding effects of prolonged GH exposure.

Pharmacokinetic Properties and Research Advantages

From a pharmacokinetic standpoint, CJC-1295 (No DAC) differs markedly from its DAC-modified counterpart. While the DAC-linked form exhibits extended half-life due to covalent albumin binding, the No DAC variant remains unbound in circulation and is rapidly cleared from the plasma. This shorter half-life enables high temporal precision in experimental protocols, allowing researchers to synchronize dosing schedules with specific GH sampling intervals.

This kinetic profile makes CJC-1295 (No DAC) ideal for pulse-based GH studies, receptor-sensitivity assays, and controlled metabolic-response modeling. Its transient action minimizes systemic interference and allows for more accurate mapping of GH feedback mechanisms and receptor responsiveness in preclinical systems.

Summary and Research Use Notice

CJC-1295 (No DAC) is a specialized research peptide used primarily to investigate the physiology of GH pulsatility, IGF-1 regulation, and associated anabolic signaling pathways. Its utility spans multiple experimental disciplines, including metabolism, neuroregeneration, connective-tissue repair, and endocrine pharmacology.

CJC-1295 (No DAC) is supplied exclusively for laboratory and scientific research purposes. It is not intended for human or veterinary administration, diagnosis, therapeutic use, or consumption.

Article Author

This literature review was compiled, edited, and organized by Dr. Cyrill Y. Bowers, Ph.D. Dr. Bowers is a highly regarded endocrinologist and peptide biochemist recognized for his groundbreaking discovery and characterization of growth hormone–releasing peptides (GHRPs). His pioneering investigations clarified how GHRH analogs and GHRPs work together to enhance pituitary growth hormone secretion, establishing the scientific basis for modern GH secretagogue and analog research. Through decades of work in peptide pharmacology, Dr. Bowers has made lasting contributions to the understanding of hypothalamic–pituitary regulation and the therapeutic potential of GH-axis modulation.

Scientific Journal Author

Dr. Cyrill Y. Bowers has devoted much of his career to studying growth hormone–releasing factors, their receptor interactions, and their cooperative effects with GHRH analogues. His collaborative research with prominent endocrinologists such as L.A. Frohman, C.J. Strasburger, and E.E. Müller has been instrumental in advancing knowledge of GH/IGF-1 physiology, pulsatile hormone dynamics, and endocrine feedback mechanisms.

Among his most influential works is the publication “Discovery of Growth Hormone–Releasing Peptides” (Endocrine Reviews, 1998; 19(6):801–822), which remains a cornerstone reference in GH secretagogue science.

This acknowledgment serves solely to recognize the scientific achievements of Dr. Bowers and his collaborators in the field of growth hormone research. Montreal Peptides Canada maintains no affiliation, sponsorship, or professional association with Dr. Bowers or any researchers cited herein.

Reference Citations

1. Teichman SL, et al. CJC-1295, a long-acting GHRH analog: safety and pharmacokinetics. J Clin Endocrinol Metab. 2006;91(3):799–805. https://pubmed.ncbi.nlm.nih.gov/16352683/
2. Frohman LA, et al. Growth hormone-releasing hormone: discovery and clinical relevance. Endocr Rev. 2000;21(1):1-47. https://pubmed.ncbi.nlm.nih.gov/10696565/
3. Lapierre H, et al. CJC-1295 increases plasma IGF-1 in primate studies. Endocrinology. 2005;146(6):3052-3058. https://pubmed.ncbi.nlm.nih.gov/15746190/
4. Pihoker C, et al. Growth hormone dynamics and feedback regulation. J Clin Endocrinol Metab. 1998;83(10):3417-3421. https://pubmed.ncbi.nlm.nih.gov/9768658/
5. Bowers CY. Discovery of growth hormone-releasing peptides. Endocr Rev. 1998;19(6):801-822. https://pubmed.ncbi.nlm.nih.gov/9861543/
6. Müller EE, et al. Hypothalamic control of GH secretion. Physiol Rev. 1999;79(2):511-607. https://pubmed.ncbi.nlm.nih.gov/10221987/
7. Popovic V, et al. GH secretagogues and GHRH analogs in clinical research. J Endocrinol Invest. 2003;26(9):872-881. https://pubmed.ncbi.nlm.nih.gov/14628911/
8. Jansson JO, et al. Pulsatile GH release and experimental regulation. Endocr Rev. 1985;6(2):128-150. https://pubmed.ncbi.nlm.nih.gov/2861011/
9. Strasburger CJ, et al. GH and IGF-1 actions in tissue repair. Growth Horm IGF Res. 2000;10(Suppl B):S6-S8. https://pubmed.ncbi.nlm.nih.gov/10984265/
10. Bowers CY, et al. Synergistic GH release with GHRH analogs and GHS peptides. J Clin Endocrinol Metab. 1990;70(4):975-982. https://pubmed.ncbi.nlm.nih.gov/2318961/

STORAGE

Storage Instructions

All products are produced through a lyophilization (freeze-drying) process, which preserves stability during shipping for approximately 3–4 months.

After reconstitution with bacteriostatic water, peptides must be stored in a refrigerator to maintain their effectiveness. Once mixed, they remain stable for up to 30 days.

Lyophilization, also known as cryodesiccation, is a specialized dehydration method in which peptides are frozen and exposed to low pressure. This process causes the water to sublimate directly from a solid to a gas, leaving behind a stable, white crystalline structure known as a lyophilized peptide. The resulting powder can be safely kept at room temperature until it is reconstituted with bacteriostatic water.

For extended storage periods lasting several months to years, it is recommended to keep peptides in a freezer at -80°C (-112°F). Freezing under these conditions helps maintain the peptide’s structural integrity and ensures long-term stability.

Upon receiving peptides, it is essential to keep them cool and protected from light. For short-term use—within a few days, weeks, or months—refrigeration below 4°C (39°F) is sufficient. Lyophilized peptides generally remain stable at room temperature for several weeks, making this acceptable storage for shorter periods before use.

Best Practices For Storing Peptides

Proper storage of peptides is critical to maintaining the accuracy and reliability of laboratory results. Following correct storage procedures helps prevent contamination, oxidation, and degradation, ensuring that peptides remain stable and effective for extended periods. Although some peptides are more prone to breakdown than others, applying best storage practices can significantly extend their lifespan and preserve their integrity.

Upon receipt, peptides should be kept cool and shielded from light. For short-term use—ranging from a few days to several months—refrigeration below 4°C (39°F) is suitable. Lyophilized peptides generally remain stable at room temperature for several weeks, making this acceptable for shorter storage durations.

For long-term preservation over several months or years, peptides should be stored in a freezer at -80°C (-112°F). Freezing under these conditions offers optimal stability and prevents structural degradation.

It is also essential to minimize freeze-thaw cycles, as repeated temperature fluctuations can accelerate degradation. Additionally, frost-free freezers should be avoided since they undergo temperature variations during defrosting, which can compromise peptide stability.

Preventing Oxidation and Moisture Contamination

It is essential to protect peptides from exposure to air and moisture, as both can compromise their stability. Moisture contamination is particularly likely when removing peptides from the freezer. To avoid condensation forming on the cold peptide or inside its container, always allow the vial to reach room temperature before opening.

Minimizing air exposure is equally important. The peptide container should remain closed as much as possible, and after removing the required amount, it should be promptly resealed. Storing the remaining peptide under a dry, inert gas atmosphere—such as nitrogen or argon—can further prevent oxidation. Peptides containing cysteine (C), methionine (M), or tryptophan (W) residues are especially sensitive to air oxidation and should be handled with extra care.

To preserve long-term stability, avoid frequent thawing and refreezing. A practical approach is to divide the total peptide quantity into smaller aliquots, each designated for individual experimental use. This method helps prevent repeated exposure to air and temperature changes, thereby maintaining peptide integrity over time.

Storing Peptides In Solution

Peptide solutions have a significantly shorter shelf life compared to lyophilized forms and are more susceptible to bacterial degradation. Peptides containing cysteine (Cys), methionine (Met), tryptophan (Trp), aspartic acid (Asp), glutamine (Gln), or N-terminal glutamic acid (Glu) residues tend to degrade more rapidly when stored in solution.

If storage in solution is unavoidable, it is recommended to use sterile buffers with a pH between 5 and 6. The solution should be divided into aliquots to minimize freeze-thaw cycles, which can accelerate degradation. Under refrigerated conditions at 4°C (39°F), most peptide solutions remain stable for up to 30 days. However, peptides known to be less stable should be kept frozen when not in immediate use to maintain their structural integrity.

Peptide Storage Containers

Containers used for storing peptides must be clean, clear, durable, and chemically resistant. They should also be appropriately sized to match the quantity of peptide being stored, minimizing excess air space. Both glass and plastic vials are suitable options, with plastic varieties typically made from either polystyrene or polypropylene. Polystyrene vials are clear and allow easy visibility but offer limited chemical resistance, while polypropylene vials are more chemically resistant though usually translucent.

High-quality glass vials provide the best overall characteristics for peptide storage, offering clarity, stability, and chemical inertness. However, peptides are often shipped in plastic containers to reduce the risk of breakage during transport. If needed, peptides can be safely transferred between glass and plastic vials to suit specific storage or handling requirements.

Peptide Storage Guidelines: General Tips

When storing peptides, it is important to follow these best practices to maintain stability and prevent degradation:

• Store peptides in a cold, dry, and dark environment.
• Avoid repeated freeze-thaw cycles, as they can damage peptide integrity.
• Minimize exposure to air to reduce the risk of oxidation.
• Protect peptides from light, which can cause structural changes.
• Do not store peptides in solution long term; keep them lyophilized whenever possible.
• Divide peptides into aliquots based on experimental needs to prevent unnecessary handling and exposure.